The structures of many proteins have been extensively studied, however it has proved extremely difficult to investigate the structures of the mRNA molecules that carry the genetic information for these proteins.
How did life first originate on this planet? Even the most minimal cell needs three subsystems: to convey information, to create compartments, and to catalyse metabolic reactions.
Dynactin is a protein complex that activates the dynein motor protein, enabling intracellular transport. It is extremely flexible and has proved very difficult to study by conventional crystallography methods. Now for the first time, research carried out by Andrew Carter and his group in the LMB’s Structural Studies Division, has revealed the structure of this large dynactin complex, using electron cryo-microscopy (cryo-EM).
A research team from the LMB’s Cell Biology division, working with colleagues from the Structural Studies division, has revealed how cells are able to find and tag for degradation the partially synthesised proteins generated when ribosomes occasionally stall.
Cells make more than a hundred thousand new proteins every minute. Once in a while, one of the ribosomes making these proteins stalls, leaving an unfinished protein fragment.